TitleThe promyelocytic leukemia zinc finger (PLZF) protein binds DNA in a high molecular weight complex associated with cdc2 kinase.
Publication TypeJournal Article
Year of Publication1999
AuthorsBall, H J., Melnick A, Shaknovich R, Kohanski R A., and Licht J D.
JournalNucleic Acids Res
Date Published1999 Oct 15
KeywordsAnimals, Base Sequence, Binding Sites, CDC2 Protein Kinase, Chromosomes, Human, Pair 11, Chromosomes, Human, Pair 17, COS Cells, DNA, DNA-Binding Proteins, Humans, Kruppel-Like Transcription Factors, Macromolecular Substances, Molecular Sequence Data, Molecular Weight, Promyelocytic Leukemia Zinc Finger Protein, Transcription Factors, Translocation, Genetic, Tumor Cells, Cultured, Zinc Fingers

<p>A binding site selection from a CpG island library for the promyelocytic leukemia zinc finger protein (PLZF) identified two high affinity PLZF binding sites. These sequences also bound RARalpha/PLZF, a fusion protein formed in chromosomal translocation t(11;17)(q23;q21) associated with acute promyelocytic leukemia. PLZF bound DNA as a slowly migrating complex with an estimated mol. wt of 600 kDa whose formation was dependent on the POZ/dimerization domain of PLZF. The PLZF-DNA complex was unable to form in the presence of cdc2 antibodies. A PLZF-cdc2 interaction was further demonstrated by co-immunoprecipitation and a biotin-streptavidin pull-down assay. PLZF is a phosphoprotein and immunoprecipi-tates with a cdc2-like kinase activity. The PLZF-DNA complex was abolished with the addition of a phosphatase. These studies suggest that the activity of PLZF, a regulator of the cell cycle, may be modulated by cell cycle proteins. RARalpha/PLZF did not complex with cdc2, this potentially contributing to its aberrant transcriptional properties and potential role in leukemo-genesis.</p>

Alternate JournalNucleic Acids Res
PubMed ID10497277
PubMed Central IDPMC148680
Grant ListCA59936 / CA / NCI NIH HHS / United States
K08 CA73762 / CA / NCI NIH HHS / United States